pkc-ζ

PKC-ε Translocation Inhibitor Peptide is a selective modulator that controls the FcγR-mediated internalization rate of opsonized beads without affecting FcαR trafficking [1].

PKC β pseudosubstrate acetate (PKC β pseudosubstrate acetate (172308-76-8 Free base)) is a selective cell-permeable inhibitor of PKC.

Delcasertib acetate is a selective δ protein kinase C (δPKC) inhibitor for the study of acute myocardial infarction and pain.

Myristoylated TFA Pep2m (Myr-Pep2m TFA) is a cell-permeable peptide that effectively disrupts the interactions between the protein kinase ζ (PKMζ) downstream targets—N-ethylmaleimide-sensitive factor/glutamate receptor subunit 2 (NSF/GluR2). PKMζ, an autonomously active isozyme of protein kinase C (PKC), plays a crucial role in these interactions [1] [2].

Delcasertib (KAI-9803) is a potent and selective inhibitor of δ-protein kinase C (δPKC).

Epsilon-V1-2 has been extensively investigated for its function as a PKC epsilon (PKCε) inhibitor. Epsilon-V1-2 has been widely applied in studies addressing ovarian aging, apoptosis in human granulosa cells, cerebral ischemia-reperfusion injury, brain development, hepatocyte insulin signaling, and neuronal cell death under ischemic conditions. Epsilon-V1-2 has been shown to effectively reduce PKCε activity, thereby enabling detailed exploration of regulatory pathways involving mitochondrial dynamics, calcium overload, AKT activation, brain atrophy, insulin resistance, and ferroptosis. Epsilon-V1-2 demonstrates notable therapeutic relevance in models of stroke, SHORT syndrome, hepatic steatosis, and brain injury, supporting its continued evaluation as a potential pharmacological agent across multiple disease contexts.

Delcasertib (KAI-9803) hydrochloride, a potent and selective δ-protein kinase C (δPKC) inhibitor, shows promise in reducing ischemia and reperfusion injury in animal models of acute myocardial infarction (MI) [1] [2].

PKC β pseudosubstrate TFA is a selective, cell-permeable inhibitor of PKC [1].

Malantide TFA, a synthetic dodecapeptide, originates from the phosphorylation site targeted by cAMP-dependent protein kinase (PKA) on the β-subunit of phosphorylase kinase. Exhibiting a high specificity for PKA with a Michaelis constant (Km) of 15 μM, this compound demonstrates more than 90% inhibition of substrate phosphorylation in the presence of protein inhibitor (PKI) across various rat tissue extracts [1]. Moreover, Malantide TFA acts as an effective substrate for Protein Kinase C (PKC) with a Km of 16 μM [2].

Protein Kinase C (19-31) TFA is a peptide inhibitor derived from the pseudo-substrate regulatory domain of PKCa (residues 19-31), featuring a serine substitution for alanine at position 25. It serves as a substrate peptide for evaluating Protein Kinase C (PKC) activity, playing a crucial role in modulating protein functions by phosphorylating the hydroxyl groups of serine and threonine amino acids on target proteins [1] [2].

Myelin Basic Protein (MHP4-14) TFA, a synthetic peptide comprising residues 4-14 of myelin basic protein, serves as a highly selective substrate for protein kinase C (PKC) with a K_m of 7 μM. It is not phosphorylated by cyclic AMP-dependent protein kinase, casein kinases I and II, Ca^2+/calmodulin-dependent protein kinase II, or phosphorylase kinase, making it an ideal candidate for protein kinase C assays in crude tissue extracts, ensuring minimal background interference [1] [2].

N-Myristoyl-Lys-Arg-Thr-Leu-Arg is a protein kinase C (PKC) inhibitor (IC50 = 75 μM) that effectively inhibits IL-2 receptor induction and IL-2 production in the human leukemic cell line Jurkat [1].

RNAENFDRF (βIIPKC624-632) conjugated to TAT47-57, a cell-permeable peptide, forms SAMβA, a rationally designed peptide that selectively antagonizes Mfn1-βIIPKC association. SAMβA acts as a selective inhibitor of mitofusin 1-βIIPKC association, demonstrating improved heart failure outcomes in rats [1].

[Glycogen Synthase (1-12) Ala9,10, Lys11,12] is a selective substrate for protein kinase C (PKC) phosphorylation. It serves to assess PKC activity [1].

Protein Kinase C (alpha) Peptide (TFA) is a PKC-α-associated peptide functioning as a lipid-dependent serine/threonine protein kinase. It plays a pivotal role in regulating several cellular functions such as survival, proliferation, differentiation, migration, and adhesion [1].

Phosphate acceptor peptide acts as a substrate for cAMP-dependent protein kinase (PKA) and serves as a weak inhibitor of protein kinase C (PKC) [1].

FKKSFKL-NH2 is a selective peptide for protein kinase C, employed in biochemical research [1].

H-Arg-Gly-Tyr-Ala-Leu-Gly-OH is a competitive inhibitor of cAMP-dependent protein kinase [1].

PKCδ Peptide Substrate is a highly specific substrate for the δ-type of Protein kinase C, composed of a sequence that mirrors murine eEF-1α (422-443) and includes Thr-431 [1].

Protein Kinase C (661-671), a fragment peptide of the β1 subspecies of Protein Kinase C (PKC), is instrumental in regulating cellular growth and has been implicated in tumor promotion [1] [2].

Protein Kinase C βII V5 peptide (660-673) (PKC βII (660-673)) exhibits an affinity for binding to RACK1 [1].

Protein Kinase C (19-35) Peptide, acting as a PKC pseudosubstrate inhibitor/region, can potentially inhibit PKC activity by blocking the substrate-binding site within the kinase domain, thereby inactivating the cytoplasmic form of PKC [1] [2].

pTH-Related Protein (1-40) (human, mouse, rat) enhances calcium absorption in rat intestinal cells by activating the PTHR1 receptor and the PKCα/β signaling pathways. This compound also increases the expression of the parathyroid hormone 1 receptor (PTHR1) and four key proteins involved in transcellular calcium transport: potential vanillin member 6 (TRPV6), calcium-binding protein-D9K (CaBP-D9k), sodium-calcium exchanger 1 (NCX1), and plasma membrane calcium ATPase 1 (PMCA1) [1].

SAMβA TFA, a selective antagonist of Mfn1-βIIPKC association conjugated to the cell permeable peptide TAT47-57, is a rationally designed inhibitor that improves heart failure outcomes in rats [1].